Abstract:
:We have characterized glucocerebrosidase in various cell types of peripheral blood of control subjects and in cultured human blastoid cells. The intracellular level of glucocerebrosidase in cultured blastoid cells (10-30 nmol substrate hydrolyzed/h.mg protein) resembles closely values observed for leukocyte cell types and various tissues and is significantly lower than that observed in cultured fibroblasts (150-500 nmol substrate hydrolyzed/h.mg protein). Glucocerebrosidase is extracted from leukocyte cell types and cultured blastoid cells almost exclusively in a monomeric, nonactivated form with enzymatic properties identical to those of the tissue enzyme. In contrast, extracts of platelets are rich in an aggregated, activated form of the enzyme. Glucocerebrosidase in blood cells and cultured blastoid cells is heterogeneous with respect to Mr and pI due to a heterogeneous oligosaccharide composition of the enzyme. The different forms seen represent intermediates in the biosynthesis and maturation of the enzyme. Blastoid cells should thus be an attractive model system for studying the natural history of glucocerebrosidase in a cell type related to those cells involved in the pathology of Gaucher disease.
journal_name
Exp Cell Resjournal_title
Experimental cell researchauthors
Aerts JM,Heikoop J,van Weely S,Donker-Koopman WE,Barranger JA,Tager JM,Schram AWdoi
10.1016/0014-4827(88)90472-7subject
Has Abstractpub_date
1988-08-01 00:00:00pages
391-8issue
2eissn
0014-4827issn
1090-2422journal_volume
177pub_type
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